Three-dimensional structure of a Nanobody® (modeled on the VHH with pdb-code 1U0Q, Cambillau et al). The target molecule is recognized by the surface formed by three hypervariable regions located at the top of the molecule (in green, cyan and blue). Hallmarks, amino acid residues that further differentiate a camelid VHH from a human VH, can be located at different positions within the framework regions, and here are coloured red, pink and magenta.

Home R & D Nanobody® Bibliography > High Affinity

Nanobody® Bibliography

High Affinity

Arbabi Ghahroudi M, Desmyter A, Wyns L, Hamers R, Muyldermans S.  Selection and identification of single domain antibody fragments from camel heavy-chain antibodies.  FEBS Lett. 1997 Sep 15; 414(3): 521-6.

Lauwereys M, Ghahroudi MA, Desmyter A, Kinne J, Hölzer W, De Genst E, Wyns L, Muyldermans S.  Potent enzyme inhibitors derived from dromedary heavy-chain antibodies.  EMBO J. 1998 Jul 1; 17(13): 3512-20.

Frenken LG, van der Linden RH, Hermans PW, Bos JW, Ruuls RC, de Geus B, Verrips CT.  Isolation of antigen specific llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae.  J Biotechnol. 2000 Feb 28; 78(1): 11-21.

Muyldermans S.  Single domain camel antibodies: current status.  J Biotechnol. 2001 Jun; 74 (4): 277-302.

Saerens D, Kinne J, Bosmans E, Wernery U, Muyldermans S, Conrath K.  Single domain antibodies derived from dromedary lymph node and peripheral blood lymphocytes sensing conformational variants of prostate-specific antigen.  J Biol Chem. 2004 Dec 10; 279 (50): 51965-72.

De Genst E, Silence K, Ghahroudi MA, Decanniere K, Loris R, Kinne J, Wyns L, Muyldermans S.  Strong in vivo maturation compensates for structurally restricted H3 loops in antibody repertoires.  J Biol Chem. 2005 Apr 8; 280 (14): 14114-21.

Gibbs WW.  Nanobodies.  Sci Am. 2005 Aug; 293 (2): 78-83.

Huang L, Reekmans G, Saerens D, Friedt JM, Frederix F, Francis L, Muyldermans S, Campitelli A, Van Hoof C.  Prostate-specific antigen immunosensing based on mixed self-assembled monolayers, camel antibodies and colloidal gold enhanced sandwich assays.  Biosens Bioelectron. 2005 Sep 15; 21(3):483-90.

Coppieters K, Dreier T, Silence K, Haard HD, Lauwereys M, Casteels P, Beirnaert E, Jonckheere H, Wiele CV, Staelens L, Hostens J, Revets H, Remaut E, Elewaut D, Rottiers P.  Formatted anti-tumor necrosis factor alpha VHH proteins derived from camelids show superior potency and targeting to inflamed joints in a murine model of collagen-induced arthritis.  Arthritis Rheum. 2006 Jun; 54 (6): 1856-66.